Difference between revisions of "Sandbox"

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* '''Description:''' MreC is a cell shape determining protein and is associated with the [[MreB]] cytoskeleton in ''B. subtilis'' and other rod shaped bacteria.<br/><br/>
+
* '''Description:''' glutamine-fructose-6-phosphate transaminase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Gene name'''
+
|style="background:#ABCDEF;" align="center"|'''Gene name''' glaube ich oder nicht
|''mreC''
+
|''glmS''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''gcaA, ybxD ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || cell-shape determining protein
+
|style="background:#ABCDEF;" align="center"| '''Product''' || glutamine-fructose-6-phosphate transaminase
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || cell-shape determation
+
|style="background:#ABCDEF;" align="center"|'''Function''' || cell wall synthesis
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 32 kDa, 6.248 
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=sandbox sandbox]'''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 870 bp, 290 aa
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 65 kDa, 4.796 
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[mreD]]'', ''[[mreB]]''
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1800 bp, 600 aa
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein'''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[glmM]]'', ''[[ybbU]]''
 
|-
 
|-
 +
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB11954&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|-
 
|-
 +
|colspan="2" | '''Genetic context''' <br/> [[Image:quintos.gif]]
 +
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
|colspan="2" | '''Genetic context''' <br/> [[Image:mreC_context.gif]]
+
|-
 +
|colspan="2" | '''Genetic context''' <br/> [[Image:test.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 +
|-
 +
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glmS_200277_202079_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:glmS_expression.png|500px]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
<br/><br/><br/><br/>
 +
  
 
<br/><br/>
 
<br/><br/>
 +
 +
= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[cell wall synthesis]]}},
 +
{{SubtiWiki category|[[biosynthesis of cell wall components]]}},
 +
{{SubtiWiki category|[[essential genes]]}}
 +
 +
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[glmS ribozyme]]}}
  
 
=The gene=
 
=The gene=
Line 37: Line 57:
 
=== Basic information ===
 
=== Basic information ===
  
* '''Coordinates:''' 2859062-2859931
+
* '''Locus tag:''' BSU01780
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
  
''mreC'' is essential under normal conditions [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed].  Depletion of MreC leads to a progressive increase in the width and a decrease in the length of the cell.  This shape defect is consistent with a role for ''mreC'' in cell wall synthesis during elongation and has a similar phenotype to other genes with roles in elongation like ''[[rodA]]'' and the redundant gene pair ''[[pbpA]]'' and ''pbpH'' (also known as ''[[ykuA]]''). Electron microscopy of cells depleted of MreC shows regions of the cell where a thick and irregular cell wall has accumulated [http://www.ncbi.nlm.nih.gov/pubmed/12867458 PubMed] and [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed].  ''mreC'' can be deleted provided that 0.5 M sucrose and 20 mM Magnesium is provided in the media, ''mreC'' is therefore conditionally essentail.  The phenotype of the ''mreC'' deletion in these conditions is one characterised by extreamly fat and bloated cells that tend to grow in clusters [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed].
+
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
 
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [HELLO BSU00100]
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00240&redirect=T"]
  
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/mreBCD-minCD.html]
+
* '''DBTBS entry:''' no entry
  
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10327]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10948]
 
 
 
 
= Additional information=
 
 
 
===Function===
 
 
 
MreC functions in cell wall synthesis by, together with the [[MreB]] cytoskeleton, localizing the cell wall synthetic machinery to the correct part of the cell.  MreC therefore ensures that the cell wall is made in the correct way to maintain the proper shape of the cell.
 
 
 
===MreC in other organisms===
 
 
 
MreC has been studied in other organisms where it has been shown to be important in cell shape determination.
 
 
 
*''Escherishia coli'' [http://www.ncbi.nlm.nih.gov/pubmed/15612918 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/17993535 PubMed]
 
*''Caulobacter cresentus'' [http://www.ncbi.nlm.nih.gov/pubmed/16344480 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/16344481 PubMed]
 
*''Rhodobacter spheroides'' [http://www.ncbi.nlm.nih.gov/pubmed/16484180 PubMed]
 
*''Streptomyces coelicolor'' [http://www.ncbi.nlm.nih.gov/pubmed/10954092 PubMed]
 
  
 +
=== Additional information===
  
 
=The protein=
 
=The protein=
Line 71: Line 77:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' None/ structural protein
+
* '''Catalyzed reaction/ biological activity:''' L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate (according to Swiss-Prot)
  
* '''Protein family:''' COG1793
+
* '''Protein family:'''
  
* '''Paralogous protein(s):''' None
+
* '''Paralogous protein(s):'''
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
* '''Kinetic information:''' None
+
* '''Kinetic information:'''
  
* '''Domains:''' Intracellular N-terminus, transmembrane domain, Coiled coil domain and C-terminal beta-sheet domain.
+
* '''Domains:'''  
  
* '''Modification:''' None
+
* '''Modification:'''
  
* '''Cofactor(s):''' None
+
* '''Cofactor(s):'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' Interacts with [[MreD]], and a subset of the PBPs [http://www.ncbi.nlm.nih.gov/pubmed/17427287 PubMed]
+
* '''[[SubtInteract|Interactions]]:'''
  
* '''Localization:''' GFP-MreC localises to the cell membrane in a helical pattern [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed].
+
* '''[[Localization]]:'''
 +
** cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [HELLO BSU00100]
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00240&redirect=T BSU00240]
  
* '''Structure:-'''
+
* '''Structure:'''
** 2J5U: MreC from ''Lysteria monocytogenes'' [http://www.ncbi.nlm.nih.gov/pubmed/17427287 PubMed]
+
**[http://www.pdb.org/pdb/explore/explore.do?structureId=HIV2 HIV2] (from ''Bacillus subtilis'', 100% identity) {{PubMed|13454352}}
** 2QF4: MreC monomer from ''Streptococcus pneumoniae'' [http://www.ncbi.nlm.nih.gov/pubmed/17707860 PubMed]
+
** [http://www.pdb.org/pdb/explore/explore.do?structureId=2VF4 2VF4] (GlmS from ''E. coli'', 39% identity, 58% similarity) {{PubMed|18295797}}
** 2QF5: MreC dimer from ''Streptococcus pneumoniae'' [http://www.ncbi.nlm.nih.gov/pubmed/17707860 PubMed]
+
** the ribozyme: [http://www.rcsb.org/pdb/explore.do?structureId=3g8s 3G8S], [http://www.rcsb.org/pdb/explore.do?structureId=3G9C 3G9C], [http://www.rcsb.org/pdb/explore.do?structureId=3g8t 3G8T], [http://www.rcsb.org/pdb/explore.do?structureId=3g95 3G95], [http://www.rcsb.org/pdb/explore.do?structureId=3g96 3G96] (all for the ribozyme from ''Bacillus anthracis''), [http://www.rcsb.org/pdb/explore.do?structureId=2HO7 2HO7] (the ribozyme from ''Thermonanaerobacter tengcongensis'')
  
* '''Swiss prot entry:''' Q01466
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39754 P39754]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU28020]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU01780]
  
* '''E.C. number:'''
+
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.6.1.16 2.6.1.16]
  
 
=== Additional information===
 
=== Additional information===
  
 +
:* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 
=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''[[mreB]]-[[mreC]]-[[mreD]]-[[minC]]-[[minD]]''
+
* '''Operon:''' ''[[ybbP]]-[[ybbR]]-[[glmM]]-[[glmS]]''
  
* '''[[Sigma factor]]:''' [[SigH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8459776 PubMed]
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=glmS_200277_202079_1 glmS] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:''' [[SigA]] {{PubMed|22211522}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** repressed by glucosamine, N-acetylglucosamine, N-propionylglucosamine or N-formylglucosamine {{PubMed|14343123}}
 +
** ''glmS'' is only expressed in the absence of glucosamine 6-phosphate ([[glmS]] [[ribozyme]])
  
* '''Regulatory mechanism:'''  
+
* '''Regulatory mechanism:''' ''glmS'' [[ribozyme]]: glucosamine 6-phosphate binds the leader mRNA, and a [[riboswitch]] with [[ribozyme]] activity cleaves off the ''[[glmS]]'' section from the mRNA, resulting in stopp of transcript elongation
  
* '''Additional information:'''
+
* '''Additional information:'''  
 +
** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 +
** A [[ncRNA]] is predicted between ''[[glmM]]'' and ''[[glmS]]'' {{PubMed|20525796}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2000 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 4000 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' A non-polar inframe deletion strain named 3481 and a xylose dependent conditional mutant named 3461 is avaliable from the [[Errington]] lab [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed].
+
* '''Mutant:'''
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
Line 128: Line 146:
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
* '''GFP fusion:''' A functional N-terminal GFP fusion has been made where the fusion protein is the only copy of the gene in the cell: strain 3417 [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed].
+
* '''GFP fusion:'''
  
 
* '''two-hybrid system:'''  
 
* '''two-hybrid system:'''  
  
* '''Antibody:''' antisera raised in rabit is avaliable from the [[Errington]] lab.
+
* '''Antibody:'''
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
  
[[Jeff Errington]], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/jeff.errington homepage]
+
[[Wade Winkler]], University of Texas, USA, [http://www.utsouthwestern.edu/findfac/professional/0,,68018,00.html Homepage]
 
 
[[Peter Graumann]], Freiburg University, Germany [http://www.biologie.uni-freiburg.de/data/bio2/graumann/index.htm homepage]
 
  
 
=Your additional remarks=
 
=Your additional remarks=
  
''mreC'' is an abbreviation of murein region e, gene C
+
=References=
 +
==Reviews==
 +
<pubmed> 18279655 </pubmed>
  
=References=
+
==The ''glmS'' Ribozyme==
 +
<pubmed>18079181 ,16484375, 16784238 ,15096624 , 16990543 ,17114942 ,16484375 , 15029187, 17283212 , 16298301, 19228039 21317896 21395279 </pubmed>
  
# Lee JC & Stewart GC (2003) Essential nature of the ''mreC'' determinant of ''Bacillus subtilis'' ''Journal of Bacteriology'' '''185(15)''': 4490-8. [http://www.ncbi.nlm.nih.gov/pubmed/12867458 PubMed]
+
==Other Original Publications==
# Leaver M & Errington J (2005) Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in ''Bacillus subtilis'' ''Molecular Microbiology'' '''57(5)''': 1196-209 [http://www.ncbi.nlm.nih.gov/pubmed/16101995 PubMed]
+
'''Additional publications:''' {{PubMed|22211522}}
# Kruse T, Bork-Jensen J & Gerdes K (2005) The morphogenetic MreBCD proteins of ''Escherichia coli'' form an essential membrane-bound complex ''Molecular Microbiology''  '''55(1)''': 78-89 [http://www.ncbi.nlm.nih.gov/pubmed/15612918 PubMed]
+
<pubmed> 14343123 17981983 ,11160890, 18295797 20525796 </pubmed>
#Bendezú FO & de Boer PA (2008) Conditional lethality, division defects, membrane involution, and endocytosis in ''mre'' and ''mrd'' shape mutants of ''Escherichia coli'' ''Journal of Bacteriology'' '''190(5)''': 1792-811 [http://www.ncbi.nlm.nih.gov/pubmed/17993535 PubMed]
+
[[Category:Protein-coding genes]]
#Divakaruni AV, Loo RR, Xie Y, Loo JA & Gober JW (2005) The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in ''Caulobacter crescentus'' ''PNAS'' '''102(51)''': 18602-7 [http://www.ncbi.nlm.nih.gov/pubmed/16344480 PubMed]
 
#Dye NA, Pincus Z, Theriot JA, Shapiro L & Gitai Z (2005) Two independent spiral structures control cell shape in Caulobacter ''PNAS'' 102(51): 18608-13.
 
#Slovak PM, Porter SL & Armitage JP (2006) Differential localization of Mre proteins with PBP2 in ''Rhodobacter sphaeroides'' ''Journal of Bacteriology'' '''188(5)''': 1691-700
 
#Burger A, Sichler K, Kelemen G, Buttner M & Wohlleben W (2000) Identification and characterization of the ''mre'' gene region of ''Streptomyces coelicolor'' A3(2). Molecular and General Genetics '''263(6)''': 1053-60
 
# van den Ent F, Leaver M, Bendezu F, Errington J, de Boer P, Löwe J. (2006) Dimeric structure of the cell shape protein MreC and its functional implications. ''Mol Microbiol.'' '''Dec;62(6):''' 1631-42.  [http://www.ncbi.nlm.nih.gov/pubmed/17427287 PubMed]
 

Latest revision as of 14:22, 29 July 2014

  • Description: glutamine-fructose-6-phosphate transaminase

Gene name glaube ich oder nicht glmS
Synonyms gcaA, ybxD
Essential yes PubMed
Product glutamine-fructose-6-phosphate transaminase
Function cell wall synthesis
Metabolic function and regulation of this protein in SubtiPathways:
sandbox
MW, pI 65 kDa, 4.796
Gene length, protein length 1800 bp, 600 aa
Immediate neighbours glmM, ybbU
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
File:Quintos.gif
This image was kindly provided by SubtiList
Genetic context
Test.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlmS expression.png
























Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

This gene is a member of the following regulons

glmS ribozyme

The gene

Basic information

  • Locus tag: BSU01780

Phenotypes of a mutant

essential PubMed

Database entries

  • BsubCyc: [HELLO BSU00100]
  • BsubCyc: "
  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • BsubCyc: [HELLO BSU00100]
  • BsubCyc: BSU00240
  • Structure:
    • HIV2 (from Bacillus subtilis, 100% identity) PubMed
    • 2VF4 (GlmS from E. coli, 39% identity, 58% similarity) PubMed
    • the ribozyme: 3G8S, 3G9C, 3G8T, 3G95, 3G96 (all for the ribozyme from Bacillus anthracis), 2HO7 (the ribozyme from Thermonanaerobacter tengcongensis)
  • KEGG entry: [2]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • repressed by glucosamine, N-acetylglucosamine, N-propionylglucosamine or N-formylglucosamine PubMed
    • glmS is only expressed in the absence of glucosamine 6-phosphate (glmS ribozyme)
  • Regulatory mechanism: glmS ribozyme: glucosamine 6-phosphate binds the leader mRNA, and a riboswitch with ribozyme activity cleaves off the glmS section from the mRNA, resulting in stopp of transcript elongation
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • A ncRNA is predicted between glmM and glmS PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2000 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 4000 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Wade Winkler, University of Texas, USA, Homepage

Your additional remarks

References

Reviews

Philippe Durand, Béatrice Golinelli-Pimpaneau, Stéphane Mouilleron, Bernard Badet, Marie-Ange Badet-Denisot
Highlights of glucosamine-6P synthase catalysis.
Arch Biochem Biophys: 2008, 474(2);302-17
[PubMed:18279655] [WorldCat.org] [DOI] (I p)


The glmS Ribozyme

Krista M Brooks, Ken J Hampel
Rapid steps in the glmS ribozyme catalytic pathway: cation and ligand requirements.
Biochemistry: 2011, 50(13);2424-33
[PubMed:21395279] [WorldCat.org] [DOI] (I p)

Peter Y Watson, Martha J Fedor
The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo.
Nat Struct Mol Biol: 2011, 18(3);359-63
[PubMed:21317896] [WorldCat.org] [DOI] (I p)

Jesse C Cochrane, Sarah V Lipchock, Kathryn D Smith, Scott A Strobel
Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme.
Biochemistry: 2009, 48(15);3239-46
[PubMed:19228039] [WorldCat.org] [DOI] (I p)

Jennifer A Collins, Irnov Irnov, Stephanie Baker, Wade C Winkler
Mechanism of mRNA destabilization by the glmS ribozyme.
Genes Dev: 2007, 21(24);3356-68
[PubMed:18079181] [WorldCat.org] [DOI] (P p)

Rebecca A Tinsley, Jennifer R W Furchak, Nils G Walter
Trans-acting glmS catalytic riboswitch: locked and loaded.
RNA: 2007, 13(4);468-77
[PubMed:17283212] [WorldCat.org] [DOI] (P p)

Kenneth Blount, Izabela Puskarz, Robert Penchovsky, Ronald Breaker
Development and application of a high-throughput assay for glmS riboswitch activators.
RNA Biol: 2006, 3(2);77-81
[PubMed:17114942] [WorldCat.org] [DOI] (I p)

Daniel J Klein, Adrian R Ferré-D'Amaré
Structural basis of glmS ribozyme activation by glucosamine-6-phosphate.
Science: 2006, 313(5794);1752-6
[PubMed:16990543] [WorldCat.org] [DOI] (I p)

Ken J Hampel, Melissa M Tinsley
Evidence for preorganization of the glmS ribozyme ligand binding pocket.
Biochemistry: 2006, 45(25);7861-71
[PubMed:16784238] [WorldCat.org] [DOI] (P p)

Adam Roth, Ali Nahvi, Mark Lee, Inbal Jona, Ronald R Breaker
Characteristics of the glmS ribozyme suggest only structural roles for divalent metal ions.
RNA: 2006, 12(4);607-19
[PubMed:16484375] [WorldCat.org] [DOI] (P p)

Tom J McCarthy, Melissa A Plog, Shennen A Floy, Joshua A Jansen, Juliane K Soukup, Garrett A Soukup
Ligand requirements for glmS ribozyme self-cleavage.
Chem Biol: 2005, 12(11);1221-6
[PubMed:16298301] [WorldCat.org] [DOI] (P p)

Jeffrey E Barrick, Keith A Corbino, Wade C Winkler, Ali Nahvi, Maumita Mandal, Jennifer Collins, Mark Lee, Adam Roth, Narasimhan Sudarsan, Inbal Jona, J Kenneth Wickiser, Ronald R Breaker
New RNA motifs suggest an expanded scope for riboswitches in bacterial genetic control.
Proc Natl Acad Sci U S A: 2004, 101(17);6421-6
[PubMed:15096624] [WorldCat.org] [DOI] (P p)

Wade C Winkler, Ali Nahvi, Adam Roth, Jennifer A Collins, Ronald R Breaker
Control of gene expression by a natural metabolite-responsive ribozyme.
Nature: 2004, 428(6980);281-6
[PubMed:15029187] [WorldCat.org] [DOI] (I p)


Other Original Publications

Additional publications: PubMed

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Stéphane Mouilleron, Marie-Ange Badet-Denisot, Béatrice Golinelli-Pimpaneau
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel.
J Mol Biol: 2008, 377(4);1174-85
[PubMed:18295797] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

K Yoshida, K Kobayashi, Y Miwa, C M Kang, M Matsunaga, H Yamaguchi, S Tojo, M Yamamoto, R Nishi, N Ogasawara, T Nakayama, Y Fujita
Combined transcriptome and proteome analysis as a powerful approach to study genes under glucose repression in Bacillus subtilis.
Nucleic Acids Res: 2001, 29(3);683-92
[PubMed:11160890] [WorldCat.org] [DOI] (I p)

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